ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O13309

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ADH2_PICST
Primary accession number O13309
Secondary accession numbers A3LQC2 O00090
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 48)
Name and origin of the protein
Protein name Alcohol dehydrogenase 2
Synonyms EC 1.1.1.1
Alcohol dehydrogenase II
ADH 1
Gene name
Name: ADH2
Synonyms: ADH1
ORFNames: PICST_27980
From
Pichia stipitis (Yeast) [TaxID: 4924] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545;
PubMed=9546172 [NCBI, ExPASy, EBI, Israel, Japan]
Cho J.Y., Jeffries T.W.;
"Pichia stipitis genes for alcohol dehydrogenase with fermentative and respiratory functions.";
Appl. Environ. Microbiol. 64:1350-1358(1998).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 62970 / CBS 5774 / NRRL Y-11542;
DOI=10.1002/(SICI)1097-0061(1998100)14:14<1311::AID-YEA315>3.3.CO;2-K; PubMed=9802210 [NCBI, ExPASy, EBI, Israel, Japan]
Passoth V., Schaefer B., Liebel B., Weierstall T., Klinner U.;
"Molecular cloning of alcohol dehydrogenase genes of the yeast Pichia stipitis and identification of the fermentative ADH.";
Yeast 14:1311-1325(1998).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545;
DOI=10.1038/nbt1290; PubMed=17334359 [NCBI, ExPASy, EBI, Israel, Japan]
Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.;
"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis.";
Nat. Biotechnol. 25:319-326(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF008244; AAC49990.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13238; CAA73690.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000496; ABN65181.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_001383210.1; -.
3D structure databases
HSSP P39462; 1JVB. [HSSP ENTRY / PDB]
SMR O13309; 2-348.
ModBase O13309.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00059; ADH_ZINC; 1.
BLOCKS O13309.
Genome annotation databases
GeneID 4837414; -.
KEGG pic:PICST_27980; -.
Other
ProtoNet O13309.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   348  348     Alcohol dehydrogenase 2. PRO_0000160728
METAL   44    44        Zinc 1; catalytic (By similarity). 
METAL   67    67        Zinc 1; catalytic (By similarity). 
METAL   98    98        Zinc 2 (By similarity). 
METAL   101   101        Zinc 2 (By similarity). 
METAL   104   104        Zinc 2 (By similarity). 
METAL   112   112        Zinc 2 (By similarity). 
METAL   154   154        Zinc 1; catalytic (By similarity). 
CONFLICT   41    41        Missing (in Ref. 2; CAA73690). 
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 36565 Da [This is the MW of the unprocessed precursor] CRC64: F6C813C98F56A148 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSIPTTQKAV IFETNGGPLL YKDIPVPKPK PNELLINVKY SGVCHTDLHA WKGDWPLDTK 

        70         80         90        100        110        120 
LPLVGGHEGA GVVVALGENV TGWEIGDYAG IKWINGSCLQ CEYCVTAHES NCPDADLSGY 

       130        140        150        160        170        180 
THDGSFQQYA TADAIQAARI PKGTDLALIA PILCAGITVY KALKTAQLQA GQWVAVSGAA 

       190        200        210        220        230        240 
GGLGSLAIQY AKAMGYRVVG IDGGADKGEF AKSLGAEVFV DFLSSKDVVA DVLKATNGGA 

       250        260        270        280        290        300 
HGVINVSVSE RAMQQSVDYV RPTGTVVLVG LPAGAKVSAS VFSSVVRTIQ IKGSYVGNRA 

       310        320        330        340 
DSAEAIDFFT RGLIKCPIKI VGLSELASVY ELMEQGKILG RYVVDTSK
O13309 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!